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Protein

Histone H1x

Gene

H1FX

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Histones H1 are necessary for the condensation of nucleosome chains into higher-order structures.

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL
  • DNA binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1x
Gene namesi
Name:H1FX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

HGNCiHGNC:4722. H1FX.

Subcellular locationi

GO - Cellular componenti

  • cell-cell adherens junction Source: BHF-UCL
  • nucleolus Source: HPA
  • nucleosome Source: InterPro
  • nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29099.

Polymorphism and mutation databases

BioMutaiH1FX.
DMDMi6016184.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 213212Histone H1xPRO_0000195912Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineCombined sources1 Publication
Modified residuei2 – 21PhosphoserineCombined sources
Modified residuei31 – 311PhosphoserineCombined sources
Modified residuei33 – 331PhosphoserineCombined sources
Modified residuei47 – 471N6-acetyllysineCombined sources
Modified residuei62 – 621CitrullineBy similarity

Post-translational modificationi

Citrullination at Arg-62 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.By similarity

Keywords - PTMi

Acetylation, Citrullination, Phosphoprotein

Proteomic databases

EPDiQ92522.
MaxQBiQ92522.
PaxDbiQ92522.
PeptideAtlasiQ92522.
PRIDEiQ92522.
TopDownProteomicsiQ92522.

PTM databases

iPTMnetiQ92522.
PhosphoSiteiQ92522.

Expressioni

Tissue specificityi

Expressed ubiquitously.

Gene expression databases

BgeeiENSG00000184897.
CleanExiHS_H1FX.
GenevisibleiQ92522. HS.

Organism-specific databases

HPAiCAB012235.
HPA040099.

Interactioni

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi114461. 51 interactions.
DIPiDIP-36358N.
IntActiQ92522. 32 interactions.
MINTiMINT-5009259.
STRINGi9606.ENSP00000329662.

Structurei

Secondary structure

1
213
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi47 – 5913Combined sources
Helixi67 – 748Combined sources
Turni82 – 843Combined sources
Helixi85 – 9814Combined sources
Beta strandi101 – 1055Combined sources
Beta strandi107 – 1093Combined sources
Beta strandi111 – 1166Combined sources
Turni120 – 1223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LSONMR-A44-123[»]
ProteinModelPortaliQ92522.
SMRiQ92522. Positions 44-123.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini44 – 11875H15PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the histone H1/H5 family.PROSITE-ProRule annotation
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00730000111536.
HOGENOMiHOG000112842.
HOVERGENiHBG009035.
InParanoidiQ92522.
KOiK11275.
OMAiATHKKGA.
OrthoDBiEOG091G167M.
PhylomeDBiQ92522.
TreeFamiTF313664.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q92522-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSVELEEALP VTTAEGMAKK VTKAGGSAAL SPSKKRKNSK KKNQPGKYSQ
60 70 80 90 100
LVVETIRRLG ERNGSSLAKI YTEAKKVPWF DQQNGRTYLK YSIKALVQND
110 120 130 140 150
TLLQVKGTGA NGSFKLNRKK LEGGGERRGA PAAATAPAPT AHKAKKAAPG
160 170 180 190 200
AAGSRRADKK PARGQKPEQR SHKKGAGAKK DKGGKAKKTA AAGGKKVKKA
210
AKPSVPKVPK GRK
Length:213
Mass (Da):22,487
Last modified:February 1, 1997 - v1
Checksum:i11548D85C5448FF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64142 mRNA. Translation: BAA11018.1.
BC000426 mRNA. Translation: AAH00426.1.
BC010435 mRNA. Translation: AAH10435.1.
CCDSiCCDS3057.1.
PIRiJC4928.
RefSeqiNP_006017.1. NM_006026.3.
UniGeneiHs.75307.

Genome annotation databases

EnsembliENST00000333762; ENSP00000329662; ENSG00000184897.
GeneIDi8971.
KEGGihsa:8971.
UCSCiuc003elx.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D64142 mRNA. Translation: BAA11018.1.
BC000426 mRNA. Translation: AAH00426.1.
BC010435 mRNA. Translation: AAH10435.1.
CCDSiCCDS3057.1.
PIRiJC4928.
RefSeqiNP_006017.1. NM_006026.3.
UniGeneiHs.75307.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2LSONMR-A44-123[»]
ProteinModelPortaliQ92522.
SMRiQ92522. Positions 44-123.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114461. 51 interactions.
DIPiDIP-36358N.
IntActiQ92522. 32 interactions.
MINTiMINT-5009259.
STRINGi9606.ENSP00000329662.

PTM databases

iPTMnetiQ92522.
PhosphoSiteiQ92522.

Polymorphism and mutation databases

BioMutaiH1FX.
DMDMi6016184.

Proteomic databases

EPDiQ92522.
MaxQBiQ92522.
PaxDbiQ92522.
PeptideAtlasiQ92522.
PRIDEiQ92522.
TopDownProteomicsiQ92522.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000333762; ENSP00000329662; ENSG00000184897.
GeneIDi8971.
KEGGihsa:8971.
UCSCiuc003elx.3. human.

Organism-specific databases

CTDi8971.
GeneCardsiH1FX.
HGNCiHGNC:4722. H1FX.
HPAiCAB012235.
HPA040099.
MIMi602785. gene.
neXtProtiNX_Q92522.
PharmGKBiPA29099.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00730000111536.
HOGENOMiHOG000112842.
HOVERGENiHBG009035.
InParanoidiQ92522.
KOiK11275.
OMAiATHKKGA.
OrthoDBiEOG091G167M.
PhylomeDBiQ92522.
TreeFamiTF313664.

Miscellaneous databases

ChiTaRSiH1FX. human.
GeneWikiiH1FX.
GenomeRNAii8971.
PROiQ92522.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000184897.
CleanExiHS_H1FX.
GenevisibleiQ92522. HS.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiH1X_HUMAN
AccessioniPrimary (citable) accession number: Q92522
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: February 1, 1997
Last modified: September 7, 2016
This is version 149 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.